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Database: UniProt
Entry: Q0CMV8_ASPTN
LinkDB: Q0CMV8_ASPTN
Original site: Q0CMV8_ASPTN 
ID   Q0CMV8_ASPTN            Unreviewed;      1275 AA.
AC   Q0CMV8;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   20-JUN-2018, entry version 77.
DE   SubName: Full=Alcohol dehydrogenase I {ECO:0000313|EMBL:EAU34045.1};
GN   ORFNames=ATEG_04976 {ECO:0000313|EMBL:EAU34045.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU34045.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
RA   White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C.,
RA   Denning D.W., Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CH476600; EAU34045.1; -; Genomic_DNA.
DR   RefSeq; XP_001214154.1; XM_001214154.1.
DR   ProteinModelPortal; Q0CMV8; -.
DR   STRING; 33178.CADATEAP00004668; -.
DR   EnsemblFungi; EAU34045; EAU34045; ATEG_04976.
DR   GeneID; 4321088; -.
DR   EuPathDB; FungiDB:ATEG_04976; -.
DR   OMA; FRTINIK; -.
DR   OrthoDB; EOG092C10AB; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007963};
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN       45    378       PKS_ER. {ECO:0000259|SMART:SM00829}.
SQ   SEQUENCE   1275 AA;  138574 MW;  C5053A3AC4AD0CAC CRC64;
     MAHFPFNSCA ELCTGLKDTP VSPLPLSYVS RSPTSGINPI LSRTHKLRSE CYSARDVPNS
     RVSMGPGPGE ILVNIKYSGV CRSDLHIWKG DYPIRGKEDL IGGHEGAGVV VAIGDGVEDI
     EIGEHVGVQW INGSCGKCEA CARDGDILRC GKPSYSGGTV DGTFQEYCIC KARSAVRIPK
     DYDLELAAPV LCAGVTSYKA ILECEAHAGD LVGAGGGLGS LACQYAKALG YRVLAISSGE
     EKHRLCIDQL GAEYFVDYKR SKDIVSEVRS IEPDGPHAVV VVASTMEPFQ TALQYVRFGG
     TVVMVGLPPG GVIAADVMQM VFRTINIKAS YVGTRAETEK ALEIFFTKTF FAPFQTVELK
     DLPLVFNRMQ EGDSNMILHD YLLKNSQLRL IGCCNELNAG YAADGYARTS PTKVSVVIVP
     YMVGGLSILN AICGACSDRL KVIVISGCPN SDSVASSTLL HHTHAPGGKD QALNAFKGVT
     VAALRLNPSE RPREALDNAL AQCLESSLPV YIEIPNDLVG ISCPSPRPLS ELIISPSSHD
     RGTVGAIVEL FSSASRPILV IGGLMQSCAA HPLVEALVEK LGCPVLCQPD ARLVSSFHPQ
     YYGIFWPGIV DNNTEIIQDA DLVLALGVHW GDLHTFGKFS IDPERHRLID VQYDSVHLPN
     GRSLKHSGLR DIIGNLMLSD VGTKTYATRQ ATEYLGQRSE SCMKNSSGSH LTVTSVLDNI
     QGLINEKSTI VADCGQTWFA AIRLSLPSMA TCHMQLLYAS LGWSLPATLG CQLARPEGRT
     ILLVGDGAFQ MTAQELSTMV RMRLNPIILV FNNLGYKTET VINDGPYNYI ANWRYSQFPA
     LLDEPSHAPD QYKAPPNSNP TMLCFKIMTR QDLMDAVRLV RKEPEKLAFL ELCIQPDDAC
     DDLQHLGRLV TGKSSVEPVE TASNPSMIDI PRAASLSNGP NPRYSTFTAN RLNKQLATSI
     PNGTQLPTNS TYTEHMITVA WTSENGWGDP ELVPHGPISL MPAASVLQYA TTCFEGLKVY
     RGHDGKLRLF RPLKNCARMV KSAARISLPT FDETELLELI QTLCAVDGPH ALPVDQPMGE
     LYIRPTLIGT EPYLGVKTPQ EALLVIVMSR MANFVSTTEE IKSISQGLTL SENPKDIIRA
     WPGGGLQLAT PPLVDQLILP GVTRQSILDL ARERLSPQTR LSNGTDHAVE PLDVSERKIT
     VNDVLDAADE GRLFGAFAVG TASCILPVFR IRFESREITM GEEVLPYVSA FKGWLSDILF
     GYKPSPWAVE VREEI
//
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